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2zho
From Proteopedia
(Difference between revisions)
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==Crystal structure of the regulatory subunit of aspartate kinase from Thermus thermophilus (ligand free form)== | ==Crystal structure of the regulatory subunit of aspartate kinase from Thermus thermophilus (ligand free form)== | ||
| - | <StructureSection load='2zho' size='340' side='right' caption='[[2zho]], [[Resolution|resolution]] 2.98Å' scene=''> | + | <StructureSection load='2zho' size='340' side='right'caption='[[2zho]], [[Resolution|resolution]] 2.98Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2zho]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2zho]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZHO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dt9|2dt9]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2dt9|2dt9]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ask ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ask ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zho OCA], [https://pdbe.org/2zho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zho RCSB], [https://www.ebi.ac.uk/pdbsum/2zho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zho ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/AK_THETH AK_THETH]] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.<ref>PMID:7773416</ref> <ref>PMID:16232547</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | ||
[[Category: Aspartate kinase]] | [[Category: Aspartate kinase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Kuzuyama, T]] | [[Category: Kuzuyama, T]] | ||
[[Category: Nishiyama, M]] | [[Category: Nishiyama, M]] | ||
Revision as of 17:30, 15 December 2021
Crystal structure of the regulatory subunit of aspartate kinase from Thermus thermophilus (ligand free form)
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Categories: Flavobacterium thermophilum yoshida and oshima 1971 | Aspartate kinase | Large Structures | Kuzuyama, T | Nishiyama, M | Tomita, T | Yoshida, A | Act domain | Alternative initiation | Amino-acid biosynthesis | Diaminopimelate biosynthesis | Kinase | Lysine biosynthesis | Regulatory domain | Transferase

